MODB_BPT4
ID MODB_BPT4 Reviewed; 207 AA.
AC P39423; P39422; Q38604;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=NAD--protein ADP-ribosyltransferase modB {ECO:0000255|HAMAP-Rule:MF_04142};
DE EC=2.4.2.31 {ECO:0000255|HAMAP-Rule:MF_04142, ECO:0000269|PubMed:10634320, ECO:0000269|PubMed:15489438, ECO:0000269|PubMed:16112649};
GN Name=modB {ECO:0000255|HAMAP-Rule:MF_04142}; Synonyms=mod;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9193638; DOI=10.1007/978-1-4419-8632-0_8;
RA Wilkens K., Tiemann B., Bazan J.F., Rueger W.;
RT "ADP-ribosylation and early transcription regulation by bacteriophage T4.";
RL Adv. Exp. Med. Biol. 419:71-82(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1692800; DOI=10.1016/0378-1119(90)90053-t;
RA Frazier M.W., Mosig G.;
RT "The bacteriophage T4 gene mrh whose product inhibits late T4 gene
RT expression in an Escherichia coli rpoH (sigma 32) mutant.";
RL Gene 88:7-14(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10634320;
RA Tiemann B., Depping R., Rueger W.;
RT "Overexpression, purification, and partial characterization of ADP-
RT ribosyltransferases modA and modB of bacteriophage T4.";
RL Gene Expr. 8:187-196(1999).
RN [5]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-71; ARG-73; SER-111; GLU-118;
RP PHE-129; ASN-130; TYR-131; GLU-171; GLN-172; GLU-173 AND ILE-176, AND
RP ACTIVE SITE.
RX PubMed=15489438; DOI=10.1128/jb.186.21.7262-7272.2004;
RA Tiemann B., Depping R., Gineikiene E., Kaliniene L., Nivinskas R.,
RA Ruger W.;
RT "ModA and ModB, two ADP-ribosyltransferases encoded by bacteriophage T4:
RT catalytic properties and mutation analysis.";
RL J. Bacteriol. 186:7262-7272(2004).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16112649; DOI=10.1016/j.bbrc.2005.08.023;
RA Depping R., Lohaus C., Meyer H.E., Ruger W.;
RT "The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: target
RT proteins identified.";
RL Biochem. Biophys. Res. Commun. 335:1217-1223(2005).
CC -!- FUNCTION: ADP-ribosyltransferase that regulates transcription by ADP-
CC ribosylation of host ribosomal protein S1 (PubMed:10634320). Additional
CC identified targets include proteins involved in either translation or
CC cellular metabolism such as elongation factor-Tu or trigger factor
CC (PubMed:16112649). {ECO:0000255|HAMAP-Rule:MF_04142,
CC ECO:0000269|PubMed:10634320, ECO:0000269|PubMed:16112649}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04142, ECO:0000269|PubMed:10634320,
CC ECO:0000269|PubMed:15489438, ECO:0000269|PubMed:16112649};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04142}.
CC Note=This protein is injected from the virion into the bacterial cell.
CC {ECO:0000255|HAMAP-Rule:MF_04142}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae NAD--protein ADP-
CC ribosyltransferase modA family. {ECO:0000255|HAMAP-Rule:MF_04142}.
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DR EMBL; X98695; CAA67254.1; -; Genomic_DNA.
DR EMBL; M30001; AAB07801.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42602.1; -; Genomic_DNA.
DR PIR; T10142; T10142.
DR RefSeq; NP_049636.1; NC_000866.4.
DR GeneID; 1258688; -.
DR KEGG; vg:1258688; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IDA:UniProtKB.
DR HAMAP; MF_04142; MODB_T4; 1.
DR InterPro; IPR043662; ModB-like.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase; Virion.
FT CHAIN 1..207
FT /note="NAD--protein ADP-ribosyltransferase modB"
FT /id="PRO_0000164954"
FT ACT_SITE 173
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04142,
FT ECO:0000269|PubMed:15489438"
FT BINDING 73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04142,
FT ECO:0000269|PubMed:15489438"
FT MUTAGEN 71
FT /note="L->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 73
FT /note="R->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 111
FT /note="S->A: No effect on enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 118
FT /note="E->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 129
FT /note="F->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 130
FT /note="N->A: No effect on enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 131
FT /note="Y->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 171
FT /note="E->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 172
FT /note="Q->A: No effect on enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 173
FT /note="E->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 176
FT /note="I->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
SQ SEQUENCE 207 AA; 24243 MW; 8C00DEC8503FA7EE CRC64;
MIINLADVEQ LSIKAESVDF QYDMYKKVCE KFTDFEQSVL WQCMEAKKNE ALHKHLNEII
KKHLTKSPYQ LYRGISKSTK ELIKDLQVGE VFSTNRVDSF TTSLHTACSF SYAEYFTETI
LRLKTDKAFN YSDHISDIIL SSPNTEFKYT YEDTDGLDSE RTDNLMMIVR EQEWMIPIGK
YKITSISKEK LHDSFGTFKV YDIEVVE
